PDBsum entry 2yr4

Oxidoreductase

PDB id: 2yr4

Contents

Protein chains

674 a.a. *

Ligands

FAD ×2

SO4

Waters ×1526

* Residue conservation analysis

PDB id:

2yr4

Name:

Oxidoreductase

Title:

Crystal structure of l-phenylalanine oxiase from psuedomonas sp. P-501

Structure:

Pro-enzyme of l-phenylalanine oxidase. Chain: a, b. Engineered: yes

Source:

Pseudomonas sp. P-501. Organism_taxid: 266807. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.70Å R-factor: 0.168 R-free: 0.195

Authors:

K.Ida,M.Kurabayashi,M.Suguro,H.Suzuki

Key ref:

K.Ida et al. (2008). Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501. J Biol Chem, 283, 16584-16590. PubMed id: 18417467

Date:

02-Apr-07 Release date: 15-Apr-08

Protein chains

Q5W9R9  (PAO_PSESP) -  Phenylalanine 2-monooxygenase precursor from Pseudomonas sp

Seq: 714 a.a.

Struc: 674 a.a.

Enzyme reactions

• Enzyme class: E.C.1.13.12.9 - phenylalanine 2-monooxygenase.
• Reaction: L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Biol Chem 283:16584-16590 (2008)

PubMed id: 18417467

Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501.

K.Ida, M.Kurabayashi, M.Suguro, Y.Hiruma, T.Hikima, M.Yamomoto, H.Suzuki.

ABSTRACT

The mature form of l-phenylalanine oxidase (PAOpt) from Pseudomonas sp. P-501 was generated and activated by the proteolytic cleavage of a noncatalytic proenzyme (proPAO). The crystal structures of proPAO, PAOpt, and the PAOpt-o-amino benzoate (AB) complex were determined at 1.7, 1.25, and 1.35A resolutions, respectively. The structure of proPAO suggests that the prosequence peptide of proPAO occupies the funnel (pathway) of the substrate amino acid from the outside of the protein to the interior flavin ring, whereas the funnel is closed with the hydrophobic residues at its vestibule in both PAOpt and the PAOpt-AB complex. All three structures have an oxygen channel that is open to the surface of the protein from the flavin ring. These results suggest that structural changes were induced by proteolysis; that is, the proteolysis of proPAO removes the prosequence and closes the funnel to keep the active site hydrophobic but keeps the oxygen channel open. The possibility that an interaction of the hydrophobic side chain of substrate with the residues of the vestibule region may open the funnel as a putative amino acid channel is discussed.